Information on EC 3.4.24.70 - oligopeptidase A

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.4.24.70
-
RECOMMENDED NAME
GeneOntology No.
oligopeptidase A
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-/-Gly-Pro-Ala is cleaved, but not Z-(Gly)5
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
148266-37-9
-
394250-11-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DH5
-
-
Manually annotated by BRENDA team
gene opdA
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-
Manually annotated by BRENDA team
TN3080
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
PCC 7120
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
WH 8102
-
-
Manually annotated by BRENDA team
PCC 6803
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
plants with defective enzyme expression exhibit heightened resistance to exogenous salicylate treatment; plants with defective enzyme expression exhibit heightened resistance to exogenous salicylate treatment
metabolism
isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death. TOP1 and TOP2 expression are coordinately regulated during pathogen-associated molecular pattern-triggered plant immunity; isozymes TOP1 and TOP2 are necessary for effector-triggered plant immunity via RPS2 and RPS4 resistance genes, and regulation of pathogen-triggered programmed cell death. TOP1 and TOP2 expression are coordinately regulated during pathogen-associated molecular pattern-triggered plant immunity
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Abz-GASPFRQ-EDDnp + H2O
Abz-GA + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GDSPFRQ-EDDnp + H2O
Abz-GD + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GESPFRQ-EDDnp + H2O
Abz-GE + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GFSPFRQ-EDDnp + H2O
Abz-GF + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GGSPFRQ-EDDnp + H2O
Abz-GG + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GHSPFRQ-EDDnp + H2O
Abz-GH + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GKSPFRQ-EDDnp + H2O
Abz-GK + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GLSPFRQ-EDDnp + H2O
Abz-GL + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GNSPFRQ-EDDnp + H2O
Abz-GN + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GPSPFRQ-EDDnp + H2O
Abz-GP + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GQSPFRQ-EDDnp + H2O
Abz-GQ + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GRSPFRQ-EDDnp + H2O
Abz-GR + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GSSPFRQ-EDDnp + H2O
Abz-GS + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Abz-GYSPFRQ-EDDnp + H2O
Abz-GY + SPFRQ-EDDnp
show the reaction diagram
-
-
-
-
?
Acetyl-Ala-Ala-Ala-Ala + H2O
Ala-Ala-Ala + acetyl-Ala
show the reaction diagram
alpha-casein-derived peptides + H2O
?
show the reaction diagram
-
alpha-casein is not cleaved by OpdA, but by proteases HslUV, ClpAP, or Lon, the peptide products are then cleaved by OpdA, overview
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-
?
bacteriophage P22 gp7 protein
?
show the reaction diagram
-
-
-
-
?
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
Benzyloxycarbonyl-Ala-Ala-Leu 4-nitroanilide + H2O
Benzyloxycarbonyl-Ala-Ala + Leu 4-nitroanilide
show the reaction diagram
Benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Benzyloxycarbonyl-Gly-Pro-Gly + Gly-Pro-Ala
show the reaction diagram
Bradykinin + H2O
?
show the reaction diagram
neurotensin + H2O
?
show the reaction diagram
o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
-
-
-
?
o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
best substrate for OpdA
-
-
?
o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine
?
show the reaction diagram
-
-
-
-
?
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
Prolipoprotein signal peptide + H2O
Hydrolyzed prolipoprotein signal peptide
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Bacteriophage P22 gp7 protein + H2O
?
show the reaction diagram
Prolipoprotein signal peptide + H2O
?
show the reaction diagram
additional information
?
-
-
the enzyme digests proteins to short peptides that are subsequently hydrolyzed to smaller fragments and free amino acids, protein degradation is an essential quality control and regulatory function
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
ATP-dependent protease
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
totally inhibits at 4 mM
JA-2
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totally inhibits at 0.003 mM
Pro-Ile
-
partly inhibits
salicylate
interacts with the isozyme and inhibits its peptidase activity to various degrees both in vitro and in plant extracts; interacts with the isozyme and inhibits its peptidase activity to various degrees both in vitro and in plant extracts. Specific isozyme TOP2salicylate interaction may be dependent on plant-specific modifications of isozyme TOP2
salicylic acid
inhibits the peptidase activity of isozyme TOP1 and to a lesser extent isozyme TOP2; inhibits the peptidase activity of isozyme TOP1 and to a lesser extent isozyme TOP2
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0042
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0011
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0004
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0004
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0018
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0022
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0002
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0005
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.0007
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.2
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.08
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.1
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.2
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.74
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.4
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.5
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.5
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.1
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.6
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
2.4
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
0.3
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1.5
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
595
Abz-GASPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
49
Abz-GDSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
42
Abz-GESPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1584
Abz-GFSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
194
Abz-GGSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1920
Abz-GHSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
1095
Abz-GKSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
844
Abz-GLSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
273
Abz-GNSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
159
Abz-GPSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
258
Abz-GQSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
10360
Abz-GRSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
590
Abz-GSSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
2191
Abz-GYSPFRQ-EDDnp
-
pH 7.4, 37C, recombinant wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0662
-
with o-aminobenzoyl-GFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0833
-
with o-aminobenzoyl-GFSPFR-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.0858
-
with o-aminobenzoyl-RPPGFSPFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.1129
-
with o-aminobenzoyl-GFSIFRQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
0.289
-
with o-aminobenzoyl-NKPRRPQ-N-(2,4-dinitrophenyl)-ethylenediamine as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
7.8
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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activity range, profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77100
-
gel filtration
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
in OpdA, the flexible loop is formed by residues 600-614, 600SHIFAGGYAAGYYSY614, modeling studies, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme TOP2 bound to 4-azido-salicylate, sitting-drop vapor-diffusion method, mixing of 40 mg/ml protein in 20 mM Tris, pH 8.5, 200 mM NaCl, 5 mM DTT, 5% v/v glycerol, with reservoir solution consisting of 220 mM ammonium acetate, 20% w/v PEG 3350, 20C, X-ray diffraction structure determination and analysis at 3.0 A resolution
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, in 0.25 M potassium phosphate buffer, pH 8, at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel affinity chromatography
-
recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
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recombinant His-tagged isozyme from Escherichia coli BL21 Rosetta (DE3) by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type OpdA and mutants from Escherichia coli strain DH5alpha by nickel affinity chromatography
-
to near homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli, prlC-gene; nucleotide sequences; opdA-gene; Salmonella typhimurium
expressed from pHis3-OpdA
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expression of His-tagged wild-type OpdA and mutants in Escherichia coli strain DH5alpha
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gene opdA, DNA and amino acid sequence determination and anaylsis, expression of the His-tagged enzyme in strain BL21(DE3)
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N-terminally His-tagged isozyme overexpression in Escherichia coli BL21 Rosetta (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of isozyme TOP2 is augmented by the flagellin peptide flg22 in an isozyme TOP1-dependent manner
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y607A
-
the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
Y607F
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the mutant shows altered substrate and cleavage site specificity compared to the wild-type enzyme, structure comparison with the wild-type enzyme, overview. The mutant is highly activated by NaCl in contrast to the wild-type enzyme
additional information
-
supressors of the protein-localization defect conferred by certain signal sequence mutations
Show AA Sequence (1308 entries)
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